2022
Kap-β2/Transportin mediates β-catenin nuclear transport in Wnt signaling
Hwang WY, Kostiuk V, González DP, Lusk CP, Khokha M. Kap-β2/Transportin mediates β-catenin nuclear transport in Wnt signaling. ELife 2022, 11: e70495. PMID: 36300792, PMCID: PMC9665845, DOI: 10.7554/elife.70495.Peer-Reviewed Original ResearchConceptsNuclear transport receptorsΒ-catenin nuclear transportNuclear transportΒ-cateninExcessive WntΒ-catenin nuclear importHeterologous model systemsΒ-catenin accumulatesPrimary embryonic axisNuclear transport machineryRan-dependent mannerNuclear localization signalTCF/LEF reporterPY-NLSNuclear importLocalization signalTransport machineryTransport receptorsResponsive genesEmbryonic developmentEmbryonic axisWnt signalingKey effectorsDirect bindingHuman diseases
2017
mTORC1 Balances Cellular Amino Acid Supply with Demand for Protein Synthesis through Post-transcriptional Control of ATF4
Park Y, Reyna-Neyra A, Philippe L, Thoreen CC. mTORC1 Balances Cellular Amino Acid Supply with Demand for Protein Synthesis through Post-transcriptional Control of ATF4. Cell Reports 2017, 19: 1083-1090. PMID: 28494858, PMCID: PMC5811220, DOI: 10.1016/j.celrep.2017.04.042.Peer-Reviewed Original ResearchConceptsUpstream open reading framesATF4 translationTranscriptional programsProtein synthesisEukaryotic initiation factor 2 alphaInitiation factor 2 alphaPost-transcriptional controlRapamycin complex 1Open reading frameIntegrated stress responseAmino acid transportersTranscription factor 4Translation machineryTranslation repressorProtein familyReading frameMaster regulatorPromoter elementsBioinformatics analysisResponsive mRNAsAmino acid supplyStress responseMetabolic enzymesKey effectorsAcid transportersmTORC1 balances cellular amino acid supply with demand for protein synthesis through post‐transcriptional control of ATF4
Thoreen C, Park Y. mTORC1 balances cellular amino acid supply with demand for protein synthesis through post‐transcriptional control of ATF4. The FASEB Journal 2017, 31 DOI: 10.1096/fasebj.31.1_supplement.614.32.Peer-Reviewed Original ResearchUpstream open reading framesATF4 translationTranscriptional programsProtein synthesisEukaryotic initiation factor 2 alphaInitiation factor 2 alphaPost-transcriptional controlRapamycin complex 1Open reading frameIntegrated stress responseAmino acid transportersTranscription factor 4Translation machineryTranslation repressorProtein familyReading frameMaster regulatorPromoter elementsBioinformatics analysisResponsive mRNAsAmino acid supplyStress responseMetabolic enzymesKey effectorsAcid transporters
2013
Phosphatidylcholine Transfer Protein Interacts with Thioesterase Superfamily Member 2 to Attenuate Insulin Signaling
Ersoy B, Tarun A, D’Aquino K, Hancer N, Ukomadu C, White M, Michel T, Manning B, Cohen D. Phosphatidylcholine Transfer Protein Interacts with Thioesterase Superfamily Member 2 to Attenuate Insulin Signaling. Science Signaling 2013, 6: ra64. PMID: 23901139, PMCID: PMC3959124, DOI: 10.1126/scisignal.2004111.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsGlucoseHEK293 CellsHomeostasisHumansInhibitory Concentration 50InsulinLiverMechanistic Target of Rapamycin Complex 1MiceMice, TransgenicMultiprotein ComplexesPhospholipid Transfer ProteinsPhosphorylationSignal TransductionThiolester HydrolasesTOR Serine-Threonine KinasesTuberous Sclerosis Complex 2 ProteinTumor Suppressor ProteinsConceptsThioesterase superfamily member 2Insulin receptor substrate 2Phosphatidylcholine transfer proteinTSC1-TSC2 complexGenetic ablationRapamycin complex 1Transfer proteinSteady-state amountsMember 2Hepatic glucose homeostasisPhospholipid-binding proteinProtein exhibitInsulin signalingChemical inhibitionKey effectorsSubstrate 2Mammalian targetDiet-induced diabetesProteinTSC2KnockdownGlucose homeostasisPhospholipid-dependent mechanismsActivationComplexes 1
2012
Type II p21-activated kinases (PAKs) are regulated by an autoinhibitory pseudosubstrate
Ha BH, Davis MJ, Chen C, Lou HJ, Gao J, Zhang R, Krauthammer M, Halaban R, Schlessinger J, Turk BE, Boggon TJ. Type II p21-activated kinases (PAKs) are regulated by an autoinhibitory pseudosubstrate. Proceedings Of The National Academy Of Sciences Of The United States Of America 2012, 109: 16107-16112. PMID: 22988085, PMCID: PMC3479536, DOI: 10.1073/pnas.1214447109.Peer-Reviewed Original ResearchConceptsP21-activated kinasePhosphorylated activation loopActivation loop phosphorylationCritical proline residueRho family GTPasesBcl-2/BclCellular morphological changesPAK regulationStructure-guided approachLoop phosphorylationPseudosubstrate regionAutoinhibitory pseudosubstratePseudosubstrate motifActivation loopCatalytic domainSrc SH3Cell motilityMolecular basisProline residuesKey effectorsCell deathPAK4SH3KinasePseudosubstrate
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